5n8c: Difference between revisions
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==Crystal structure of Pseudomonas aeruginosa LpxC complexed with inhibitor== | |||
<StructureSection load='5n8c' size='340' side='right' caption='[[5n8c]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5n8c]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N8C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N8C FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8Q8:(2~{S})-3-AZANYL-2-[[(1~{R})-5-[2-[4-[[2-(HYDROXYMETHYL)IMIDAZOL-1-YL]METHYL]PHENYL]ETHYNYL]-2,3-DIHYDRO-1~{H}-INDEN-1-YL]AMINO]-3-METHYL-~{N}-OXIDANYL-BUTANAMIDE'>8Q8</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-3-O-acyl-N-acetylglucosamine_deacetylase UDP-3-O-acyl-N-acetylglucosamine deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.108 3.5.1.108] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5n8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n8c OCA], [http://pdbe.org/5n8c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n8c RCSB], [http://www.ebi.ac.uk/pdbsum/5n8c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n8c ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/LPXC_PSEAE LPXC_PSEAE]] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The emergence and spread of multidrug-resistant (MDR) Gram negative bacteria presents a serious threat for public health. Novel antimicrobials that could overcome the resistance problems are urgently needed. UDP-3-O-(R-3-hydroxymyristol)-N-acetylglucosamine deacetylase (LpxC) is a cytosolic zinc-based deacetylase that catalyzes the first committed step in the biosynthesis of lipid A, which is essential for the survival of Gram-negative bacteria. Our efforts toward the discovery of novel LpxC inhibitors are presented herein. | |||
Structure-based discovery of LpxC inhibitors.,Zhang J, Chan A, Lippa B, Cross JB, Liu C, Yin N, Romero JA, Lawrence J, Heney R, Herradura P, Goss J, Clark C, Abel C, Zhang Y, Poutsiaka KM, Epie F, Conrad M, Mahamoon A, Nguyen K, Chavan A, Clark E, Li TC, Cheng RK, Wood M, Andersen OA, Brooks M, Kwong J, Barker J, Parr IB, Gu Y, Ryan MD, Coleman S, Metcalf CA 3rd Bioorg Med Chem Lett. 2017 Mar 6. pii: S0960-894X(17)30228-7. doi:, 10.1016/j.bmcl.2017.03.006. PMID:28302397<ref>PMID:28302397</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Andersen, O | <div class="pdbe-citations 5n8c" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: UDP-3-O-acyl-N-acetylglucosamine deacetylase]] | |||
[[Category: Andersen, O A]] | |||
[[Category: Barker, J]] | [[Category: Barker, J]] | ||
[[Category: Brooks, M]] | [[Category: Brooks, M]] | ||
[[Category: | [[Category: Cheng, R K]] | ||
[[Category: Cross, J | [[Category: Cross, J B]] | ||
[[Category: Kwong, J]] | [[Category: Kwong, J]] | ||
[[Category: Ryan, M D]] | |||
[[Category: Wood, M]] | [[Category: Wood, M]] | ||
[[Category: Zhang, J]] | [[Category: Zhang, J]] | ||
[[Category: Antibacterial]] | |||
[[Category: Hydrolase]] | |||
[[Category: Hyroxamate]] | |||
[[Category: Inhibitor]] | |||
[[Category: Lpxc]] | |||
Revision as of 16:47, 29 March 2017
Crystal structure of Pseudomonas aeruginosa LpxC complexed with inhibitorCrystal structure of Pseudomonas aeruginosa LpxC complexed with inhibitor
Structural highlights
Function[LPXC_PSEAE] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Publication Abstract from PubMedThe emergence and spread of multidrug-resistant (MDR) Gram negative bacteria presents a serious threat for public health. Novel antimicrobials that could overcome the resistance problems are urgently needed. UDP-3-O-(R-3-hydroxymyristol)-N-acetylglucosamine deacetylase (LpxC) is a cytosolic zinc-based deacetylase that catalyzes the first committed step in the biosynthesis of lipid A, which is essential for the survival of Gram-negative bacteria. Our efforts toward the discovery of novel LpxC inhibitors are presented herein. Structure-based discovery of LpxC inhibitors.,Zhang J, Chan A, Lippa B, Cross JB, Liu C, Yin N, Romero JA, Lawrence J, Heney R, Herradura P, Goss J, Clark C, Abel C, Zhang Y, Poutsiaka KM, Epie F, Conrad M, Mahamoon A, Nguyen K, Chavan A, Clark E, Li TC, Cheng RK, Wood M, Andersen OA, Brooks M, Kwong J, Barker J, Parr IB, Gu Y, Ryan MD, Coleman S, Metcalf CA 3rd Bioorg Med Chem Lett. 2017 Mar 6. pii: S0960-894X(17)30228-7. doi:, 10.1016/j.bmcl.2017.03.006. PMID:28302397[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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